How do pH and polyphenols affect the foaming properties of ovalbumin?

Author:

Wen Hedi1,Zhang Deju2,Ning Zhenzhen3,Li Zihao1,Zhang Yan1,Liu Jingbo1,Yu Ting4,Zhang Ting1

Affiliation:

1. Jilin Provincial Key Laboratory of Nutrition and Functional Food & College of Food Science and Engineering, Jilin University, Changchun, 130062, People's Republic of China

2. Food and Nutritional Sciences, School of Biological Sciences, The University of Hong Kong, Pokfulam Road, Hong Kong

3. Jingbrand Co. Ltd., Huangshi, Hubei, 435000, People's Republic of China

4. Department of Nutrition, the Second Hospital of Jilin University, Changchun, 130062, People's Republic of China

Abstract

Abstract To broaden the application of ovalbumin (OVA) in food formulations, it is meaningful to improve its foaming characteristics. This study aimed to investigate the effect of benzoic acid-based (3,4-dihydroxybenzoic acid, DA) and cinnamic acid-based polyphenols (trans-2-hydroxycinnamic acid, T2A) on the foaming properties of OVA at acidic (pH 3.0), neutral (pH 7.4) and alkaline (pH 9.0) pH conditions. Both the addition of polyphenols and acid treatment enhanced the foaming properties of OVA. Surface hydrophobicity, circular dichroism, free sulfhydryl groups, and Fourier transform infrared spectroscopy results indicated that after acidic workup, the presence of stronger hydrophobic interactions in OVA-polyphenol aggregates induced more disordered protein conformation and conversion or breakage of disulfide bonds. Particle size and zeta potential experiments indicated that acidic treatment neutralized protein surface charges, further inducing self-aggregation and swelling of OVA, ultimately enhancing foaming properties. Comparatively, T2A exhibited better foam-inducing capacity due to its stronger interaction with OVA, leading to the unfolding of the OVA structure and the exposure of more hydrophobic groups. The intrinsic and 3-D fluorescence spectra experiments also confirmed that OVA-T2A aggregates at pH 3.0 had greater altered non-covalent interaction forces and protein secondary and tertiary structures compared to other complexes. This study could provide a theoretical basis for designing protein formulations with excellent foaming properties.

Publisher

Research Square Platform LLC

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